Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein deglycase DJ-1

Gene

PARK7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protein deglycase that repairs methylglyoxal- and glyoxal-glycated amino acids and proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteines, arginines and lysines residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) (PubMed:25416785). Plays an important role in cell protection against oxidative stress and cell death acting as oxidative stress sensor and redox-sensitive chaperone and protease; functions probably related to its primary function (PubMed:17015834, PubMed:20304780, PubMed:18711745, PubMed:12796482, PubMed:19229105, PubMed:25416785). It is involved in neuroprotective mechanisms like the stabilization of NFE2L2 and PINK1 proteins, male fertility as a positive regulator of androgen signaling pathway as well as cell growth and transformation through, for instance, the modulation of NF-kappa-B signaling pathway (PubMed:12612053, PubMed:15502874, PubMed:14749723, PubMed:17015834, PubMed:21097510, PubMed:18711745). Its involvement in protein repair could also explain other unrelated functions. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death (PubMed:16390825). Required for correct mitochondrial morphology and function as well as for autophagy of dysfunctional mitochondria (PubMed:19229105, PubMed:16632486). Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking (PubMed:18711745). Regulates astrocyte inflammatory responses, may modulate lipid rafts-dependent endocytosis in astrocytes and neuronal cells (PubMed:23847046). Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress (PubMed:18626009). Metal-binding protein able to bind copper as well as toxic mercury ions, enhances the cell protection mechanism against induced metal toxicity (PubMed:23792957).By similarity21 Publications

Cofactori

Note: Does not require glutathione as a cofactor, however, glycated glutathione constitutes a PARK7 substrate.1 Publication

Kineticsi

kcat is 0.27 sec(-1) for the deglycation of glycated N-acetylarginine. kcat is 0.28 sec(-1) for the deglycation of glycated N-acetyllysine. kcat is 0.42 sec(-1) for the deglycation of glycated N-acetylcysteine.1 Publication

  1. KM=173.4 µM for casein1 Publication
  2. KM=0.44 mM for glycated N-acetylarginine (at pH 7.0 and 22 degrees Celsius)1 Publication
  3. KM=0.35 mM for glycated N-acetyllysine (at pH 7.0 and 22 degrees Celsius)1 Publication
  4. KM=0.32 mM for glycated N-acetylcysteine (at pH 7.0 and 22 degrees Celsius)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei106 – 1061Nucleophile2 Publications
    Active sitei126 – 12611 Publication

    GO - Molecular functioni

    • androgen receptor binding Source: ParkinsonsUK-UCL
    • copper ion binding Source: UniProtKB
    • cupric ion binding Source: ParkinsonsUK-UCL
    • cuprous ion binding Source: ParkinsonsUK-UCL
    • cytokine binding Source: ParkinsonsUK-UCL
    • enzyme binding Source: ParkinsonsUK-UCL
    • glyoxalase (glycolic acid-forming) activity Source: ParkinsonsUK-UCL
    • glyoxalase III activity Source: ParkinsonsUK-UCL
    • identical protein binding Source: IntAct
    • kinase binding Source: UniProtKB
    • L-dopa decarboxylase activator activity Source: ParkinsonsUK-UCL
    • mercury ion binding Source: UniProtKB
    • mRNA binding Source: UniProtKB
    • oxidoreductase activity, acting on peroxide as acceptor Source: ParkinsonsUK-UCL
    • peptidase activity Source: UniProtKB
    • peroxiredoxin activity Source: Ensembl
    • protein homodimerization activity Source: UniProtKB
    • receptor binding Source: UniProtKB
    • repressing transcription factor binding Source: ParkinsonsUK-UCL
    • scaffold protein binding Source: ParkinsonsUK-UCL
    • small protein activating enzyme binding Source: ParkinsonsUK-UCL
    • superoxide dismutase copper chaperone activity Source: ParkinsonsUK-UCL
    • transcription coactivator activity Source: ParkinsonsUK-UCL
    • transcription factor binding Source: ParkinsonsUK-UCL
    • tyrosine 3-monooxygenase activator activity Source: ParkinsonsUK-UCL
    • ubiquitin-like protein conjugating enzyme binding Source: ParkinsonsUK-UCL
    • ubiquitin-specific protease binding Source: ParkinsonsUK-UCL

    GO - Biological processi

    • activation of protein kinase B activity Source: ParkinsonsUK-UCL
    • adult locomotory behavior Source: Ensembl
    • autophagy Source: UniProtKB-KW
    • cellular response to glyoxal Source: ParkinsonsUK-UCL
    • cellular response to hydrogen peroxide Source: UniProtKB
    • cellular response to oxidative stress Source: ParkinsonsUK-UCL
    • detoxification of copper ion Source: UniProtKB
    • detoxification of mercury ion Source: UniProtKB
    • dopamine uptake involved in synaptic transmission Source: Ensembl
    • enzyme active site formation via L-cysteine sulfinic acid Source: Ensembl
    • glycolate biosynthetic process Source: ParkinsonsUK-UCL
    • glyoxal catabolic process Source: ParkinsonsUK-UCL
    • hydrogen peroxide metabolic process Source: ParkinsonsUK-UCL
    • inflammatory response Source: UniProtKB-KW
    • lactate biosynthetic process Source: GOC
    • membrane depolarization Source: Ensembl
    • membrane hyperpolarization Source: Ensembl
    • methylglyoxal catabolic process to D-lactate Source: ParkinsonsUK-UCL
    • mitochondrion organization Source: UniProtKB
    • negative regulation of apoptotic process Source: ParkinsonsUK-UCL
    • negative regulation of cell death Source: UniProtKB
    • negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: ParkinsonsUK-UCL
    • negative regulation of death-inducing signaling complex assembly Source: ParkinsonsUK-UCL
    • negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
    • negative regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
    • negative regulation of gene expression Source: ParkinsonsUK-UCL
    • negative regulation of hydrogen peroxide-induced cell death Source: ParkinsonsUK-UCL
    • negative regulation of hydrogen peroxide-induced neuron death Source: ParkinsonsUK-UCL
    • negative regulation of hydrogen peroxide-induced neuron intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
    • negative regulation of neuron apoptotic process Source: BHF-UCL
    • negative regulation of neuron death Source: ParkinsonsUK-UCL
    • negative regulation of oxidative stress-induced cell death Source: ParkinsonsUK-UCL
    • negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
    • negative regulation of proteasomal ubiquitin-dependent protein catabolic process Source: ParkinsonsUK-UCL
    • negative regulation of protein acetylation Source: ParkinsonsUK-UCL
    • negative regulation of protein binding Source: UniProtKB
    • negative regulation of protein export from nucleus Source: ParkinsonsUK-UCL
    • negative regulation of protein K48-linked deubiquitination Source: ParkinsonsUK-UCL
    • negative regulation of protein kinase activity Source: ParkinsonsUK-UCL
    • negative regulation of protein phosphorylation Source: ParkinsonsUK-UCL
    • negative regulation of protein sumoylation Source: ParkinsonsUK-UCL
    • negative regulation of protein ubiquitination Source: ParkinsonsUK-UCL
    • negative regulation of TRAIL-activated apoptotic signaling pathway Source: ParkinsonsUK-UCL
    • negative regulation of ubiquitin-protein transferase activity Source: ParkinsonsUK-UCL
    • negative regulation of ubiquitin-specific protease activity Source: ParkinsonsUK-UCL
    • positive regulation of androgen receptor activity Source: ParkinsonsUK-UCL
    • positive regulation of dopamine biosynthetic process Source: ParkinsonsUK-UCL
    • positive regulation of gene expression Source: ParkinsonsUK-UCL
    • positive regulation of interleukin-8 production Source: ParkinsonsUK-UCL
    • positive regulation of L-dopa biosynthetic process Source: ParkinsonsUK-UCL
    • positive regulation of L-dopa decarboxylase activity Source: ParkinsonsUK-UCL
    • positive regulation of mitochondrial electron transport, NADH to ubiquinone Source: ParkinsonsUK-UCL
    • positive regulation of mitochondrion degradation Source: ParkinsonsUK-UCL
    • positive regulation of oxidative phosphorylation uncoupler activity Source: Ensembl
    • positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: Ensembl
    • positive regulation of peptidyl-serine phosphorylation Source: ParkinsonsUK-UCL
    • positive regulation of protein homodimerization activity Source: ParkinsonsUK-UCL
    • positive regulation of protein kinase B signaling Source: ParkinsonsUK-UCL
    • positive regulation of protein localization to nucleus Source: ParkinsonsUK-UCL
    • positive regulation of pyrroline-5-carboxylate reductase activity Source: ParkinsonsUK-UCL
    • positive regulation of reactive oxygen species biosynthetic process Source: Ensembl
    • positive regulation of sequence-specific DNA binding transcription factor activity Source: ParkinsonsUK-UCL
    • positive regulation of superoxide dismutase activity Source: ParkinsonsUK-UCL
    • positive regulation of transcription from RNA polymerase II promoter Source: ParkinsonsUK-UCL
    • positive regulation of transcription regulatory region DNA binding Source: ParkinsonsUK-UCL
    • positive regulation of tyrosine 3-monooxygenase activity Source: ParkinsonsUK-UCL
    • protein deglycosylation Source: UniProtKB
    • protein stabilization Source: UniProtKB
    • Ras protein signal transduction Source: ParkinsonsUK-UCL
    • regulation of androgen receptor signaling pathway Source: UniProtKB
    • regulation of fibril organization Source: ParkinsonsUK-UCL
    • regulation of inflammatory response Source: UniProtKB
    • regulation of mitochondrial membrane potential Source: ParkinsonsUK-UCL
    • regulation of neuron apoptotic process Source: UniProtKB
    • single fertilization Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Molecular functioni

    Chaperone, Hydrolase, Protease

    Keywords - Biological processi

    Autophagy, Fertilization, Inflammatory response, Stress response

    Keywords - Ligandi

    Copper, RNA-binding

    Enzyme and pathway databases

    SignaLinkiQ99497.

    Protein family/group databases

    MEROPSiC56.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein deglycase DJ-11 Publication (EC:3.1.2.-1 Publication, EC:3.5.1.-1 Publication)
    Short name:
    DJ-1
    Alternative name(s):
    Oncogene DJ1
    Parkinson disease protein 7
    Gene namesi
    Name:PARK7Imported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:16369. PARK7.

    Subcellular locationi

    GO - Cellular componenti

    • axon Source: ParkinsonsUK-UCL
    • cell body Source: Ensembl
    • chromatin Source: ParkinsonsUK-UCL
    • cytoplasm Source: UniProtKB
    • cytosol Source: UniProtKB
    • endoplasmic reticulum Source: Ensembl
    • extracellular exosome Source: UniProtKB
    • membrane raft Source: UniProtKB-SubCell
    • mitochondrial intermembrane space Source: Ensembl
    • mitochondrial matrix Source: Ensembl
    • mitochondrion Source: UniProtKB
    • nucleus Source: UniProtKB
    • plasma membrane Source: UniProtKB-SubCell
    • PML body Source: ParkinsonsUK-UCL
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Mitochondrion, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Parkinson disease 7 (PARK7)4 Publications

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionA neurodegenerative disorder characterized by resting tremor, postural tremor, bradykinesia, muscular rigidity, anxiety and psychotic episodes. PARK7 has onset before 40 years, slow progression and initial good response to levodopa. Some patients may show traits reminiscent of amyotrophic lateral sclerosis-parkinsonism/dementia complex (Guam disease).

    See also OMIM:606324
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti26 – 261M → I in PARK7; does not affect protein stability and degradation; does not interfere with homodimerization. 2 Publications
    VAR_020492
    Natural varianti64 – 641E → D in PARK7; no apparent effect on protein stability; impaired mitochondrial morphology. 3 Publications
    VAR_020493
    Natural varianti104 – 1041A → T in PARK7; Loss of protection against metal cytotoxicity. 2 Publications
    VAR_020495
    Natural varianti149 – 1491D → A in PARK7; Loss of protection against metal cytotoxicity. 2 Publications
    Corresponds to variant rs74315352 [ dbSNP | Ensembl ].
    VAR_020496
    Natural varianti166 – 1661L → P in PARK7; strongly decreases enzymatic activity; reduces protein stability and leads to increased degradation; ubiquitinated by PARK2 leading to its recognition by HDAC6 and targeting to aggresome where is degraded; interferes with homodimerization; abolishes interaction with PIAS2; strongly reduces chaperone activity; decreases PINK1 steady-state level; reduced localization in lipid rafts. 8 Publications
    Corresponds to variant rs28938172 [ dbSNP | Ensembl ].
    VAR_020498

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi18 – 181E → A: Strongly decreases enzymatic activity. 1 Publication
    Mutagenesisi18 – 181E → D: Strongly decreases enzymatic activity. 1 Publication
    Mutagenesisi18 – 181E → N: Strongly decreases enzymatic activity. 1 Publication
    Mutagenesisi18 – 181E → Q: Strongly decreases enzymatic activity. 1 Publication
    Mutagenesisi46 – 461C → A: Reduced localization in lipid rafts; when associated with A-106. 4 Publications
    Mutagenesisi46 – 461C → A: Reduces protein stability. No effect on oxidation. 4 Publications
    Mutagenesisi46 – 461C → S: No effect on mitochondrial translocation neither on deglycase activity. 5 Publications
    Mutagenesisi51 – 511V → A: Disrupts dimer formation and strongly reduces ability to eliminate hydrogen peroxide. 1 Publication
    Mutagenesisi53 – 531C → A: Strongly reduces chaperone activity and ability to eliminate hydrogen peroxide. 4 Publications
    Mutagenesisi53 – 531C → S: No effect on mitochondrial translocation neither on deglycase activity. 5 Publications
    Mutagenesisi106 – 1061C → A: Abolishes enzymatic activity. Abolishes oxidation, association with mitochondria and protease activity. No effect on chaperone activity. Reduced binding to OTUD7B. 8 Publications
    Mutagenesisi106 – 1061C → A: Reduced localization in lipid rafts; when associated with A-46. 7 Publications
    Mutagenesisi106 – 1061C → D: Abolishes oxidation and association with mitochondria. No effect on chaperone activity. 7 Publications
    Mutagenesisi106 – 1061C → S: Loss of deglycase activity. No effect on mitochondrial translocation. Reduced protease activity. No effect on protection against metal cytotoxicity. 8 Publications
    Mutagenesisi126 – 1261H → A: Strongly decreases enzymatic activity. 2 Publications
    Mutagenesisi130 – 1301K → R: Partially compensates for loss of stability; when associated with P-166. 1 Publication

    Keywords - Diseasei

    Disease mutation, Neurodegeneration, Parkinson disease, Parkinsonism, Tumor suppressor

    Organism-specific databases

    MIMi168600. phenotype.
    606324. phenotype.
    Orphaneti90020. Amyotrophic lateral sclerosis-parkinsonism-dementia complex.
    2828. Young adult-onset Parkinsonism.
    PharmGKBiPA32946.

    Polymorphism and mutation databases

    BioMutaiPARK7.
    DMDMi56404943.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei? – 189Removed in mature formPRO_0000405558
    Chaini1 – ?Protein deglycase DJ-1PRO_0000157849

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi46 – 461S-palmitoyl cysteine1 Publication
    Lipidationi53 – 531S-palmitoyl cysteine1 Publication
    Modified residuei67 – 671Phosphotyrosine1 Publication
    Modified residuei106 – 1061Cysteine sulfinic acid (-SO2H); alternate1 Publication
    Lipidationi106 – 1061S-palmitoyl cysteine; alternate1 Publication
    Cross-linki130 – 130Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
    Modified residuei148 – 1481N6-acetyllysineBy similarity
    Modified residuei182 – 1821N6-succinyllysineBy similarity

    Post-translational modificationi

    Sumoylated on Lys-130 by PIAS2 or PIAS4; which is enhanced after ultraviolet irradiation and essential for cell-growth promoting activity and transforming activity.1 Publication
    Cys-106 is easily oxidized to sulfinic acid.2 Publications
    Undergoes cleavage of a C-terminal peptide and subsequent activation of protease activity in response to oxidative stress.1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Lipoprotein, Oxidation, Palmitate, Phosphoprotein, Ubl conjugation, Zymogen

    Proteomic databases

    PaxDbiQ99497.
    PeptideAtlasiQ99497.
    PRIDEiQ99497.

    2D gel databases

    OGPiQ99497.
    REPRODUCTION-2DPAGEIPI00298547.
    UCD-2DPAGEO14805.
    Q99497.

    PTM databases

    PhosphoSiteiQ99497.

    Miscellaneous databases

    PMAP-CutDBQ99497.

    Expressioni

    Tissue specificityi

    Highly expressed in pancreas, kidney, skeletal muscle, liver, testis and heart. Detected at slightly lower levels in placenta and brain (at protein level). Detected in astrocytes, Sertoli cells, spermatogonia, spermatids and spermatozoa.4 Publications

    Inductioni

    By hydrogen peroxide and UV irradiation.2 Publications

    Gene expression databases

    BgeeiQ99497.
    CleanExiHS_PARK7.
    ExpressionAtlasiQ99497. baseline and differential.
    GenevisibleiQ99497. HS.

    Organism-specific databases

    HPAiCAB005870.
    HPA004190.

    Interactioni

    Subunit structurei

    Homodimer (PubMed:12851414, PubMed:12796482, PubMed:12855764). Binds EFCAB6/DJBP and PIAS2 (PubMed:11477070, PubMed:12851414, PubMed:12612053). Part of a ternary complex containing PARK7, EFCAB6/DJBP and AR (PubMed:12612053). Interacts (via N-terminus) with OTUD7B (PubMed:21097510). Interacts with BBS1, HIPK1, CLCF1 and MTERF (PubMed:16390825, PubMed:21097510). Forms a complex with PINK1 and PARK2 (PubMed:19229105).7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-1164361,EBI-1164361
    ARP102756EBI-1164361,EBI-608057
    DAXXQ9UER73EBI-1164361,EBI-77321
    FADDQ131589EBI-1164361,EBI-494804
    GNB2L1P632444EBI-1164361,EBI-296739
    GOPCQ9HD263EBI-1164361,EBI-349832
    MTA2O947763EBI-1164361,EBI-1783035
    OTUD7BQ6GQQ93EBI-1164361,EBI-527784
    PYCR1P323225EBI-1164361,EBI-848624

    Protein-protein interaction databases

    BioGridi116446. 62 interactions.
    DIPiDIP-35515N.
    IntActiQ99497. 39 interactions.
    MINTiMINT-5003468.
    STRINGi9606.ENSP00000340278.

    Structurei

    Secondary structure

    1
    189
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 106Combined sources
    Helixi16 – 2813Combined sources
    Beta strandi32 – 376Combined sources
    Turni38 – 414Combined sources
    Beta strandi47 – 493Combined sources
    Beta strandi51 – 533Combined sources
    Beta strandi55 – 573Combined sources
    Helixi58 – 625Combined sources
    Beta strandi68 – 725Combined sources
    Helixi76 – 849Combined sources
    Helixi86 – 9712Combined sources
    Beta strandi101 – 1055Combined sources
    Turni106 – 1083Combined sources
    Helixi109 – 1146Combined sources
    Helixi127 – 1293Combined sources
    Helixi130 – 1334Combined sources
    Turni134 – 1363Combined sources
    Beta strandi139 – 1413Combined sources
    Beta strandi145 – 1495Combined sources
    Beta strandi152 – 1554Combined sources
    Helixi158 – 1603Combined sources
    Helixi161 – 17313Combined sources
    Helixi175 – 1828Combined sources
    Helixi183 – 1853Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1J42X-ray2.50A1-189[»]
    1P5FX-ray1.10A1-189[»]
    1PDVX-ray1.80A1-189[»]
    1PDWX-ray2.20A/B/C/D/E/F/G/H1-189[»]
    1PE0X-ray1.70A/B1-189[»]
    1Q2UX-ray1.60A1-189[»]
    1SOAX-ray1.20A1-189[»]
    1UCFX-ray1.95A/B1-189[»]
    2OR3X-ray1.20A/B1-189[»]
    2R1TX-ray1.70A/B2-188[»]
    2R1UX-ray1.50A/B2-188[»]
    2R1VX-ray1.70A/B2-188[»]
    2RK3X-ray1.05A1-189[»]
    2RK4X-ray1.15A1-189[»]
    2RK6X-ray1.15A1-189[»]
    3B36X-ray1.50A1-189[»]
    3B38X-ray1.85A1-189[»]
    3B3AX-ray1.50A1-189[»]
    3BWEX-ray2.40A/B/C/D/E/F/G1-189[»]
    3CY6X-ray1.35A1-189[»]
    3CYFX-ray1.60A1-189[»]
    3CZ9X-ray1.15A1-189[»]
    3CZAX-ray1.20A1-189[»]
    3EZGX-ray1.15A1-189[»]
    3F71X-ray1.20A1-189[»]
    3SF8X-ray1.56A/B1-189[»]
    4BTEX-ray1.38A1-189[»]
    4MNTX-ray1.58A1-189[»]
    4MTCX-ray1.47A1-189[»]
    4N0MX-ray1.95A1-189[»]
    4N12X-ray1.48A1-189[»]
    4OGFX-ray1.60A2-188[»]
    4OQ4X-ray1.49A1-189[»]
    4P2GX-ray1.35A1-189[»]
    4P34X-ray1.55A1-189[»]
    4P35X-ray1.75A1-189[»]
    4P36X-ray1.18A1-189[»]
    4ZGGX-ray1.23A1-189[»]
    ProteinModelPortaliQ99497.
    SMRiQ99497. Positions 3-188.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99497.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C56 family.Curated

    Phylogenomic databases

    eggNOGiCOG0693.
    GeneTreeiENSGT00390000001231.
    HOGENOMiHOG000063194.
    HOVERGENiHBG053511.
    InParanoidiQ99497.
    KOiK05687.
    OMAiMAGDHYK.
    OrthoDBiEOG7CVPZX.
    PhylomeDBiQ99497.
    TreeFamiTF300119.

    Family and domain databases

    Gene3Di3.40.50.880. 1 hit.
    InterProiIPR029062. Class_I_gatase-like.
    IPR006287. DJ1.
    IPR002818. ThiJ/PfpI.
    [Graphical view]
    PfamiPF01965. DJ-1_PfpI. 1 hit.
    [Graphical view]
    SUPFAMiSSF52317. SSF52317. 1 hit.
    TIGRFAMsiTIGR01383. not_thiJ. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q99497-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MASKRALVIL AKGAEEMETV IPVDVMRRAG IKVTVAGLAG KDPVQCSRDV
    60 70 80 90 100
    VICPDASLED AKKEGPYDVV VLPGGNLGAQ NLSESAAVKE ILKEQENRKG
    110 120 130 140 150
    LIAAICAGPT ALLAHEIGFG SKVTTHPLAK DKMMNGGHYT YSENRVEKDG
    160 170 180
    LILTSRGPGT SFEFALAIVE ALNGKEVAAQ VKAPLVLKD
    Length:189
    Mass (Da):19,891
    Last modified:July 5, 2004 - v2
    Checksum:i4B21661B3A76BC67
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti119 – 1191F → C in BAB71782 (Ref. 3) Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti26 – 261M → I in PARK7; does not affect protein stability and degradation; does not interfere with homodimerization. 2 Publications
    VAR_020492
    Natural varianti39 – 391A → S Probable disease-associated mutation found in early-onset Parkinson disease with digenic inheritance; the patient also carries PINK1 mutation L-399. 1 Publication
    VAR_072589
    Natural varianti64 – 641E → D in PARK7; no apparent effect on protein stability; impaired mitochondrial morphology. 3 Publications
    VAR_020493
    Natural varianti98 – 981R → Q.4 Publications
    Corresponds to variant rs71653619 [ dbSNP | Ensembl ].
    VAR_020494
    Natural varianti104 – 1041A → T in PARK7; Loss of protection against metal cytotoxicity. 2 Publications
    VAR_020495
    Natural varianti149 – 1491D → A in PARK7; Loss of protection against metal cytotoxicity. 2 Publications
    Corresponds to variant rs74315352 [ dbSNP | Ensembl ].
    VAR_020496
    Natural varianti150 – 1501G → S.1 Publication
    VAR_020497
    Natural varianti163 – 1631E → K.1 Publication
    VAR_034801
    Natural varianti166 – 1661L → P in PARK7; strongly decreases enzymatic activity; reduces protein stability and leads to increased degradation; ubiquitinated by PARK2 leading to its recognition by HDAC6 and targeting to aggresome where is degraded; interferes with homodimerization; abolishes interaction with PIAS2; strongly reduces chaperone activity; decreases PINK1 steady-state level; reduced localization in lipid rafts. 8 Publications
    Corresponds to variant rs28938172 [ dbSNP | Ensembl ].
    VAR_020498
    Natural varianti171 – 1711A → S.1 Publication
    VAR_020499

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D61380 mRNA. Translation: BAA09603.2.
    AF021819 mRNA. Translation: AAC12806.1.
    AB073864 mRNA. Translation: BAB71782.1.
    AK312000 mRNA. Translation: BAG34938.1.
    AL034417 Genomic DNA. Translation: CAB52550.1.
    CH471130 Genomic DNA. Translation: EAW71591.1.
    BC008188 mRNA. Translation: AAH08188.1.
    AB045294 Genomic DNA. No translation available.
    AY648999 Genomic DNA. Translation: AAT68961.1.
    CCDSiCCDS93.1.
    PIRiJC5394.
    RefSeqiNP_001116849.1. NM_001123377.1.
    NP_009193.2. NM_007262.4.
    XP_005263481.1. XM_005263424.2.
    UniGeneiHs.419640.

    Genome annotation databases

    EnsembliENST00000338639; ENSP00000340278; ENSG00000116288.
    ENST00000377488; ENSP00000366708; ENSG00000116288.
    ENST00000377491; ENSP00000366711; ENSG00000116288.
    ENST00000493373; ENSP00000465404; ENSG00000116288.
    ENST00000493678; ENSP00000418770; ENSG00000116288.
    GeneIDi11315.
    KEGGihsa:11315.
    UCSCiuc001aou.4. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    SHMPD

    The Singapore human mutation and polymorphism database

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D61380 mRNA. Translation: BAA09603.2.
    AF021819 mRNA. Translation: AAC12806.1.
    AB073864 mRNA. Translation: BAB71782.1.
    AK312000 mRNA. Translation: BAG34938.1.
    AL034417 Genomic DNA. Translation: CAB52550.1.
    CH471130 Genomic DNA. Translation: EAW71591.1.
    BC008188 mRNA. Translation: AAH08188.1.
    AB045294 Genomic DNA. No translation available.
    AY648999 Genomic DNA. Translation: AAT68961.1.
    CCDSiCCDS93.1.
    PIRiJC5394.
    RefSeqiNP_001116849.1. NM_001123377.1.
    NP_009193.2. NM_007262.4.
    XP_005263481.1. XM_005263424.2.
    UniGeneiHs.419640.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1J42X-ray2.50A1-189[»]
    1P5FX-ray1.10A1-189[»]
    1PDVX-ray1.80A1-189[»]
    1PDWX-ray2.20A/B/C/D/E/F/G/H1-189[»]
    1PE0X-ray1.70A/B1-189[»]
    1Q2UX-ray1.60A1-189[»]
    1SOAX-ray1.20A1-189[»]
    1UCFX-ray1.95A/B1-189[»]
    2OR3X-ray1.20A/B1-189[»]
    2R1TX-ray1.70A/B2-188[»]
    2R1UX-ray1.50A/B2-188[»]
    2R1VX-ray1.70A/B2-188[»]
    2RK3X-ray1.05A1-189[»]
    2RK4X-ray1.15A1-189[»]
    2RK6X-ray1.15A1-189[»]
    3B36X-ray1.50A1-189[»]
    3B38X-ray1.85A1-189[»]
    3B3AX-ray1.50A1-189[»]
    3BWEX-ray2.40A/B/C/D/E/F/G1-189[»]
    3CY6X-ray1.35A1-189[»]
    3CYFX-ray1.60A1-189[»]
    3CZ9X-ray1.15A1-189[»]
    3CZAX-ray1.20A1-189[»]
    3EZGX-ray1.15A1-189[»]
    3F71X-ray1.20A1-189[»]
    3SF8X-ray1.56A/B1-189[»]
    4BTEX-ray1.38A1-189[»]
    4MNTX-ray1.58A1-189[»]
    4MTCX-ray1.47A1-189[»]
    4N0MX-ray1.95A1-189[»]
    4N12X-ray1.48A1-189[»]
    4OGFX-ray1.60A2-188[»]
    4OQ4X-ray1.49A1-189[»]
    4P2GX-ray1.35A1-189[»]
    4P34X-ray1.55A1-189[»]
    4P35X-ray1.75A1-189[»]
    4P36X-ray1.18A1-189[»]
    4ZGGX-ray1.23A1-189[»]
    ProteinModelPortaliQ99497.
    SMRiQ99497. Positions 3-188.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi116446. 62 interactions.
    DIPiDIP-35515N.
    IntActiQ99497. 39 interactions.
    MINTiMINT-5003468.
    STRINGi9606.ENSP00000340278.

    Protein family/group databases

    MEROPSiC56.002.

    PTM databases

    PhosphoSiteiQ99497.

    Polymorphism and mutation databases

    BioMutaiPARK7.
    DMDMi56404943.

    2D gel databases

    OGPiQ99497.
    REPRODUCTION-2DPAGEIPI00298547.
    UCD-2DPAGEO14805.
    Q99497.

    Proteomic databases

    PaxDbiQ99497.
    PeptideAtlasiQ99497.
    PRIDEiQ99497.

    Protocols and materials databases

    DNASUi11315.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000338639; ENSP00000340278; ENSG00000116288.
    ENST00000377488; ENSP00000366708; ENSG00000116288.
    ENST00000377491; ENSP00000366711; ENSG00000116288.
    ENST00000493373; ENSP00000465404; ENSG00000116288.
    ENST00000493678; ENSP00000418770; ENSG00000116288.
    GeneIDi11315.
    KEGGihsa:11315.
    UCSCiuc001aou.4. human.

    Organism-specific databases

    CTDi11315.
    GeneCardsiGC01P008014.
    GeneReviewsiPARK7.
    HGNCiHGNC:16369. PARK7.
    HPAiCAB005870.
    HPA004190.
    MIMi168600. phenotype.
    602533. gene.
    606324. phenotype.
    neXtProtiNX_Q99497.
    Orphaneti90020. Amyotrophic lateral sclerosis-parkinsonism-dementia complex.
    2828. Young adult-onset Parkinsonism.
    PharmGKBiPA32946.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0693.
    GeneTreeiENSGT00390000001231.
    HOGENOMiHOG000063194.
    HOVERGENiHBG053511.
    InParanoidiQ99497.
    KOiK05687.
    OMAiMAGDHYK.
    OrthoDBiEOG7CVPZX.
    PhylomeDBiQ99497.
    TreeFamiTF300119.

    Enzyme and pathway databases

    SignaLinkiQ99497.

    Miscellaneous databases

    ChiTaRSiPARK7. human.
    EvolutionaryTraceiQ99497.
    GeneWikiiPARK7.
    GenomeRNAii11315.
    NextBioi42983.
    PMAP-CutDBQ99497.
    PROiQ99497.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ99497.
    CleanExiHS_PARK7.
    ExpressionAtlasiQ99497. baseline and differential.
    GenevisibleiQ99497. HS.

    Family and domain databases

    Gene3Di3.40.50.880. 1 hit.
    InterProiIPR029062. Class_I_gatase-like.
    IPR006287. DJ1.
    IPR002818. ThiJ/PfpI.
    [Graphical view]
    PfamiPF01965. DJ-1_PfpI. 1 hit.
    [Graphical view]
    SUPFAMiSSF52317. SSF52317. 1 hit.
    TIGRFAMsiTIGR01383. not_thiJ. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "DJ-1, a novel oncogene which transforms mouse NIH3T3 cells in cooperation with ras."
      Nagakubo D., Taita T., Kitaura H., Ikeda M., Tamai K., Iguchi-Ariga S.M.M., Ariga H.
      Biochem. Biophys. Res. Commun. 231:509-513(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Cervix carcinoma.
    2. "Homo sapiens RNA-binding protein regulatory subunit mRNA."
      Beaudoin R., Hod Y.
      Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lung.
    3. "Human DJ-1 cDNA from PC3 cells."
      Ariga H., Niki T.
      Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Thalamus.
    5. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Cervix.
    8. "Molecular cloning of human and mouse DJ-1 genes and identification of Sp1-dependent activation of the human DJ-1 promoter."
      Taira T., Takahashi K., Kitagawa R., Iguchi-Ariga S.M.M., Ariga H.
      Gene 263:285-292(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
      Tissue: Kidney.
    9. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 6-27; 33-89; 99-122 AND 149-175, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    10. "DJ-1 gene G150S mutation."
      Zou H.Q., Chan P.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 138-189, VARIANT SER-150.
    11. "DJ-1 positively regulates the androgen receptor by impairing the binding of PIASx alpha to the receptor."
      Takahashi K., Taira T., Niki T., Seino C., Iguchi-Ariga S.M.M., Ariga H.
      J. Biol. Chem. 276:37556-37563(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PIAS2, SUBCELLULAR LOCATION, FUNCTION.
    12. "L166P mutant DJ-1, causative for recessive Parkinson's disease, is degraded through the ubiquitin-proteasome system."
      Miller D.W., Ahmad R., Hague S., Baptista M.J., Canet-Aviles R., McLendon C., Carter D.M., Zhu P.-P., Stadler J., Chandran J., Klinefelter G.R., Blackstone C., Cookson M.R.
      J. Biol. Chem. 278:36588-36595(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEGRADATION BY THE PROTEASOME, SUBCELLULAR LOCATION, INTERACTION WITH PIAS2, HOMODIMERIZATION, MUTAGENESIS OF LYS-130, CHARACTERIZATION OF VARIANT PARK7 PRO-166.
    13. "A missense mutation (L166P) in DJ-1, linked to familial Parkinson's disease, confers reduced protein stability and impairs homo-oligomerization."
      Moore D.J., Zhang L., Dawson T.M., Dawson V.L.
      J. Neurochem. 87:1558-1567(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEGRADATION BY THE PROTEASOME, CHARACTERIZATION OF VARIANTS PARK7 ILE-26 AND PRO-166.
    14. "DJBP: a novel DJ-1-binding protein, negatively regulates the androgen receptor by recruiting histone deacetylase complex, and DJ-1 antagonizes this inhibition by abrogation of this complex."
      Niki T., Takahashi-Niki K., Taira T., Iguchi-Ariga S.M.M., Ariga H.
      Mol. Cancer Res. 1:247-261(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EFCAB6, COMPONENT OF A COMPLEX COMPOSED OF AR; EFCAB6 AND PARK7.
    15. "Immunocytochemical localization of DJ-1 in human male reproductive tissue."
      Yoshida K., Sato Y., Yoshiike M., Nozawa S., Ariga H., Iwamoto T.
      Mol. Reprod. Dev. 66:391-397(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    16. Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    17. Cited for: TISSUE SPECIFICITY.
    18. "DJ-1 has a role in antioxidative stress to prevent cell death."
      Taira T., Saito Y., Niki T., Iguchi-Ariga S.M., Takahashi K., Ariga H.
      EMBO Rep. 5:213-218(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION, MUTAGENESIS OF VAL-51 AND CYS-53.
    19. "DJ-1 is a redox-dependent molecular chaperone that inhibits alpha-synuclein aggregate formation."
      Shendelman S., Jonason A., Martinat C., Leete T., Abeliovich A.
      PLoS Biol. 2:1-10(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-46; CYS-53 AND CYS-106.
    20. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-67, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Proper SUMO-1 conjugation is essential to DJ-1 to exert its full activities."
      Shinbo Y., Niki T., Taira T., Ooe H., Takahashi-Niki K., Maita C., Seino C., Iguchi-Ariga S.M.M., Ariga H.
      Cell Death Differ. 13:96-108(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-130, OXIDATION, SUBCELLULAR LOCATION, INDUCTION, FUNCTION.
    22. "DJ-1 interacts with HIPK1 and affects H2O2-induced cell death."
      Sekito A., Koide-Yoshida S., Niki T., Taira T., Iguchi-Ariga S.M.M., Ariga H.
      Free Radic. Res. 40:155-165(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HIPK1, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-106.
    23. "DJ-1, a cancer- and Parkinson's disease-associated protein, stabilizes the antioxidant transcriptional master regulator Nrf2."
      Clements C.M., McNally R.S., Conti B.J., Mak T.W., Ting J.P.
      Proc. Natl. Acad. Sci. U.S.A. 103:15091-15096(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    24. Cited for: FUNCTION.
    25. "Parkin, PINK1, and DJ-1 form a ubiquitin E3 ligase complex promoting unfolded protein degradation."
      Xiong H., Wang D., Chen L., Choo Y.S., Ma H., Tang C., Xia K., Jiang W., Ronai Z., Zhuang X., Zhang Z.
      J. Clin. Invest. 119:650-660(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COMPONENT OF A COMPLEX COMPOSED OF PARK2; PARK7 AND PINK1, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT PARK7 PRO-166.
    26. "Mitochondrial localization of DJ-1 leads to enhanced neuroprotection."
      Junn E., Jang W.H., Zhao X., Jeong B.S., Mouradian M.M.
      J. Neurosci. Res. 87:123-129(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-46; CYS-53 AND CYS-106.
    27. "Parkinson disease protein DJ-1 converts from a zymogen to a protease by carboxyl-terminal cleavage."
      Chen J., Li L., Chin L.S.
      Hum. Mol. Genet. 19:2395-2408(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITES, MUTAGENESIS OF CYS-106 AND HIS-126.
    28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "DJ-1 enhances cell survival through the binding of cezanne, a negative regulator of NF-{kappa}B."
      McNally R.S., Davis B.K., Clements C.M., Accavitti-Loper M.A., Mak T.W., Ting J.P.
      J. Biol. Chem. 286:4098-4106(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BBS1; CLCF1; MTERF AND OTUD7B, MUTAGENESIS OF CYS-106.
    30. Cited for: FUNCTION, CAUTION, MUTAGENESIS OF GLU-18; CYS-106 AND HIS-126, CHARACTERIZATION OF VARIANT PARK7 PRO-166.
    31. "DJ-1 associates with lipid rafts by palmitoylation and regulates lipid rafts-dependent endocytosis in astrocytes."
      Kim K.S., Kim J.S., Park J.Y., Suh Y.H., Jou I., Joe E.H., Park S.M.
      Hum. Mol. Genet. 22:4805-4817(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PALMITOYLATION AT CYS-46; CYS-53 AND CYS-106, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-46 AND CYS-106, CHARACTERIZATION OF VARIANT PARK7 PRO-166.
    32. "Parkinson disease protein DJ-1 binds metals and protects against metal-induced cytotoxicity."
      Bjorkblom B., Adilbayeva A., Maple-Grodem J., Piston D., Okvist M., Xu X.M., Brede C., Larsen J.P., Moller S.G.
      J. Biol. Chem. 288:22809-22820(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COPPER-BINDING, CHARACTERIZATION OF VARIANTS PARK7 THR-104 AND ALA-149, MUTAGENESIS OF CYS-106.
    33. "Parkinsonism-associated protein DJ-1/Park7 is a major protein deglycase that repairs methylglyoxal- and glyoxal-glycated cysteine, arginine and lysine residues."
      Richarme G., Mihoub M., Dairou J., Bui L.C., Leger T., Lamouri A.
      J. Biol. Chem. 290:1885-1897(2015) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, CAUTION, MUTAGENESIS OF CYS-46; CYS-53 AND CYS-106, COFACTOR.
    34. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    35. "Crystal structure of DJ-1/RS and implication on familial Parkinson's disease."
      Huai Q., Sun Y., Wang H., Chin L.-S., Li L., Robinson H., Ke H.
      FEBS Lett. 549:171-175(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), HOMODIMERIZATION.
    36. "Crystal structure of human DJ-1, a protein associated with early onset Parkinson's disease."
      Tao X., Tong L.
      J. Biol. Chem. 278:31372-31379(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF WILD-TYPE AND MUTANT ARG-130, HOMODIMERIZATION.
    37. "The crystal structure of DJ-1, a protein related to male fertility and Parkinson's disease."
      Honbou K., Suzuki N.N., Horiuchi M., Niki T., Taira T., Ariga H., Inagaki F.
      J. Biol. Chem. 278:31380-31384(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), HOMODIMERIZATION.
    38. "Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain."
      Lee S.-J., Kim S.J., Kim I.-K., Ko J., Jeong C.-S., Kim G.-H., Park C., Kang S.-O., Suh P.-G., Lee H.-S., Cha S.-S.
      J. Biol. Chem. 278:44552-44559(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, OXIDATION AT CYS-106, HOMODIMERIZATION.
    39. "The 1.1-A resolution crystal structure of DJ-1, the protein mutated in autosomal recessive early onset Parkinson's disease."
      Wilson M.A., Collins J.L., Hod Y., Ringe D., Petsko G.A.
      Proc. Natl. Acad. Sci. U.S.A. 100:9256-9261(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS), HOMODIMERIZATION, OXIDATION, LACK OF PROTEOLYTIC ACTIVITY.
    40. "The Parkinson's disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization."
      Canet-Aviles R.M., Wilson M.A., Miller D.W., Ahmad R., McLendon C., Bandyopadhyay S., Baptista M.J., Ringe D., Petsko G.A., Cookson M.R.
      Proc. Natl. Acad. Sci. U.S.A. 101:9103-9108(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS), MUTAGENESIS OF CYS-46; CYS-53 AND CYS-106, OXIDATION, FUNCTION, SUBCELLULAR LOCATION.
    41. "The role of pathogenic DJ-1 mutations in Parkinson's disease."
      Abou-Sleiman P.M., Healy D.G., Quinn N., Lees A.J., Wood N.W.
      Ann. Neurol. 54:283-286(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PARK7 ILE-26 AND ALA-149, VARIANT GLN-98.
    42. Cited for: VARIANT PARK7 PRO-166, SUBCELLULAR LOCATION.
    43. Cited for: VARIANT GLN-98.
    44. Cited for: VARIANT PARK7 ASP-64, X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    45. "Differential effects of Parkinson's disease-associated mutations on stability and folding of DJ-1."
      Goerner K., Holtorf E., Odoy S., Nuscher B., Yamamoto A., Regula J.T., Beyer K., Haass C., Kahle P.J.
      J. Biol. Chem. 279:6943-6951(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS PARK7 ASP-64 AND PRO-166.
    46. Cited for: VARIANT PARK7 THR-104, VARIANTS GLN-98 AND SER-171.
    47. Cited for: VARIANT GLN-98.
    48. Cited for: VARIANT LYS-163.
    49. "Association of PINK1 and DJ-1 confers digenic inheritance of early-onset Parkinson's disease."
      Tang B., Xiong H., Sun P., Zhang Y., Wang D., Hu Z., Zhu Z., Ma H., Pan Q., Xia J.-H., Xia K., Zhang Z.
      Hum. Mol. Genet. 15:1816-1825(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SER-39.
    50. "Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6."
      Olzmann J.A., Li L., Chudaev M.V., Chen J., Perez F.A., Palmiter R.D., Chin L.S.
      J. Cell Biol. 178:1025-1038(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT PARK7 PRO-166.
    51. "Reduced basal autophagy and impaired mitochondrial dynamics due to loss of Parkinson's disease-associated protein DJ-1."
      Krebiehl G., Ruckerbauer S., Burbulla L.F., Kieper N., Maurer B., Waak J., Wolburg H., Gizatullina Z., Gellerich F.N., Woitalla D., Riess O., Kahle P.J., Proikas-Cezanne T., Kruger R.
      PLoS ONE 5:E9367-E9367(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ASP-64, FUNCTION.

    Entry informationi

    Entry nameiPARK7_HUMAN
    AccessioniPrimary (citable) accession number: Q99497
    Secondary accession number(s): B2R4Z1
    , O14805, Q6DR95, Q7LFU2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 7, 2004
    Last sequence update: July 5, 2004
    Last modified: July 22, 2015
    This is version 158 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Caution

    Glyoxylase activity previously reported reflects in fact its deglycase activity (PubMed:22523093, PubMed:25416785).2 Publications

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.